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The ability of tumor cells to adhere to, migrate on, and remodel extracellular matrices is mediated by cell surface receptors such as β1-integrins. Here we conducted functional live-cell imaging in real time to investigate the effects of modulating β1-integrin expression and function on proteolytic remodeling of the extracellular matrix. Human breast and prostate cancer cells were grown on reconstituted basement membrane containing a quenched fluorescent form of collagen IV. Generation of cleavage products and the resulting increases in fluorescence were imaged and quantified. Decreases in the expression and activity of β1-integrin reduced digestion of quenched fluorescent-collagen IV by the breast and prostate cancer cells and correspondingly their invasion through and migration on reconstituted basement membrane. Decreased extracellular matrix degradation also was associated with changes in the constituents of proteolytic pathways: decreases in secretion of the cysteine protease cathepsin B, the matrix metalloproteinase (MMP)-13, and tissue inhibitors of metalloproteinases (TIMP)-1 and 2; a decrease in expression of MMP-14 or membrane type 1 MMP; and an increase in secretion of TIMP-3. This is the first study to demonstrate through functional live-cell imaging that downregulation of β1-integrin expression and function reduces proteolysis of collagen IV by breast and prostate cancer cells

Functional Live-Cell Imaging Demonstrates that β1-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells

Functional Live-Cell Imaging Demonstrates that β₁-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells